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The X-ray structure of HIV-1 protease reveals that it is composed of , each consisting of 99 amino acid residues. The subunits come together in such as way as to . This tunnel is of critical importance because the active site of the protease is located in its interior. The active site consists of , making it a member of the aspartyl protease family. The two Asp's are either interact with the incoming water OR protonate the carbonyl to make the carbon more electrophilic for the incoming . (more...)
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- October 2025: The Nobel Prize in Chemistry recognizes the development of Metal-Organic Frameworks that have a multitude of potential applications. These are similar to Metal-Ligand Polyhedra, but they form extended crystalline networks instead of discrete polyhedra.
- November 2024: How To Find A Structure is a new guide to finding an empirical model for a protein of interest, choosing which empirical structure is best, and getting an AlphaFold-predicted structure when no empirical structures are available.
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- November 2024: A handful of case studies illustrate what Nobel-Prize winning AlphaFold3 can, and cannot, predict.
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- A practical guide to teaching with Proteopedia [1]
How to display cavities, pockets, and tunnels. |
- January 2021: How to display cavities, pockets, and tunnels? Jmol/Cavities_pockets_and_tunnels
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- ↑ Castro C, Johnson RJ, Kieffer B, Means JA, Taylor A, Telford J, Thompson LK, Sussman JL, Prilusky J, Theis K. A practical guide to teaching with Proteopedia. Biochem Mol Biol Educ. 2021 Jun 3. doi: 10.1002/bmb.21548. PMID:34080750 doi:http://dx.doi.org/10.1002/bmb.21548
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